ArticleBiochimica et biophysica acta. Biomembranes2017
Probing the disparate effects of arginine and lysine residues on antimicrobial peptide/bilayer association.
Article in Biochimica et biophysica acta. Biomembranes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Bioactive Peptides in Probiotic Fermented Foods: Structure-Activity Relationships and Cardiometabolic Protective Effects.Physiological research · 2026Review
- A Comprehensive In-Silico Pipeline for the Discovery of Non-toxic, Stable Antimicrobial Peptides From Databases for Targeting Multi-Drug ResistantBioinformatics and biology insights · 2026Article
- From computational screening toFrontiers in microbiology · 2026Article
- A Bioinspired Mastoparan Exhibits Concentration-Dependent Anti-Bacterial Activity via Membrane Disruption.ACS applied materials & interfaces · 2025Article
- Enhanced Gram-Negative Membrane Disruption and In Vivo Efficacy via Lysine-Arginine Enrichment of Opis16a.ACS medicinal chemistry letters · 2025Article
- Conjugation of Polycationic Peptides Extends the Efficacy Spectrum of β-Lactam Antibiotics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Cyclization increases bactericidal activity of arginine-rich cationic cell-penetrating peptide forMicrobiology spectrum · 2024Article
- Development of a Selective and Stable Antimicrobial Peptide.ACS infectious diseases · 2024Article
- Molecular de-extinction of ancient antimicrobial peptides enabled by machine learning.Cell host & microbe · 2023Article
- Label-free measurement of antimicrobial peptide interactions with lipid vesicles and nanodiscs using microscale thermophoresis.Scientific reports · 2023Article
- Adsorption/Desorption of Cationic-Hydrophobic Peptides on Zwitterionic Lipid Bilayer Is Associated with the Possibility of Proton Transfer.Antibiotics (Basel, Switzerland) · 2023Article
- Optimization of antimicrobial peptides for the application against biocorrosive bacteria.Applied microbiology and biotechnology · 2023Article
- Initiation and evolution of pores formed by influenza fusion peptides probed by lysolipid inclusion.Biophysical journal · 2023Article
- Evolutionary andCurrent research in microbial sciences · 2023Article
- Article
- Therapeutic Potential of Antimicrobial Peptide PN5 against Multidrug-Resistant E. coli and Anti-Inflammatory Activity in a Septic Mouse Model.Microbiology spectrum · 2022Article
- The Influence of Short Motifs on the Anticancer Activity of HB43 Peptide.Pharmaceutics · 2022Article
- Exploration of the Structure-Function Relationships of a Novel Frog Skin Secretion-Derived Bioactive Peptide, t-DPH1, through Use of Rational Design, Cationicity Enhancement and In Vitro Studies.Antibiotics (Basel, Switzerland) · 2021Article
- Potential Anti-Alzheimer Agents from Guanidinyl Tryptophan Derivatives with Activities of Membrane Adhesion and Conformational Transition Inhibitions.Molecules (Basel, Switzerland) · 2021Article
- Article
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2 authors.
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Abstract
Antimicrobial peptides (AMPs) are key components of the innate immune response and represent promising templates for the development of broad-spectrum alternatives to conventional antibiotics. Most AMPs are short, cationic peptides that interact more strongly with negatively charged prokaryotic membranes than net neutral eukaryotic ones. Both AMPs and synthetic analogues with arginine-like side chains are more active against bacteria than those with lysine-like amine groups, though the atomistic mechanism for this increase in potency remains unclear. To examine this, we conducted comparative molecular dynamics simulations of a model negatively-charged membrane system interacting with two mutants of the AMP KR-12: one with lysine residues mutated to arginines (R-KR12) and one with arginine residues mutated to lysine (K-KR12). Simulations show that both partition analogously to the bilayer and display similar preferences for hydrogen bonding with the anionic POPGs. However, R-KR12 binds stronger to the bilayer than K-KR12 and forms significantly more hydrogen bonds, leading to considerably longer interaction times. Additional simulations with methylated R-KR12 and charge-modified K-KR12 mutants show that the extensive interaction seen in the R-KR12 system is partly due to arginine's strong atomic charge distribution, rather than being purely an effect of the greater number of hydrogen bond donors. Finally, free energy simulations reveal that both peptides are disordered in solution but form an amphipathic α-helix when inserted into the bilayer headgroup region. Overall, these results highlight the role of charge and hydrogen bond strength in peptide bilayer insertion, and offer potential insights for designing more potent analogues in the future.
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